Доклады Академии наукДоклады Академии наук0869-5652The Russian Academy of Sciences1345110.31857/S0869-56524862255-257Research ArticleThapsigargin, inhibitor of sarco-endoplasmic Ca2+-ATPase, effectively suppresses the expression of S100A4 in human breast cancer cell lineKotnovaA. P.alina_kotnova@mail.ruLyanovaB. M.alina_kotnova@mail.ruDukhaninaE. A.alina_kotnova@mail.ruPortsevaT. N.alina_kotnova@mail.ruIlyinYu. V.<p>Academician of the Russian Academy of Sciences</p>alina_kotnova@mail.ruGeorgievaS. G.<p>Corresponding Member of the Russian Academy of Sciences</p>alina_kotnova@mail.ruStepchenkoA. G.alina_kotnova@mail.ruPankratovaE. V.alina_kotnova@mail.ruEngelhardt Institute of Molecular Biology of the Russian Academy of Sciences2705201948622552571606201916062019Copyright © 2019, Russian academy of sciences2019<p>Thapsigargin, the SERCA ATPase inhibitor, effectively suppresses the expression of metastasis marker S100A4 in breast cancer cells MDA-MB231. It has been demonstrated that transcription of the <em>S100A4</em> gene is controlled by Ca<sup>2+</sup>-signaling pathways. It has been shown that synthesis of S100A4 mRNA and protein in the MDA-MB231 cell line is effectively inhibited by thapsigargin at a concentration of 0.4-4 M, while preserving cell survival. We assume that a change in gene transcription in response to the disruption of Ca<sup>2+</sup> homeostasis plays a direct role in the remodeling of Ca<sup>2+</sup>-signaling pathways.</p>S100A4inhibitorsthapsigarginmetastasisS100A4ингибиторытапсигаргинметастазирование[Stewart R. L., Carpenter B. L., West D. S., Knifley T., Liu L., Wang C., Weiss H. L., Gal T. S., Durbin E. B., Arnold S. M., O’Connor K.L., Chen M. // Oncotarget. 2016. V. 7. № 23. P. 34630-34642.][Helfman D. M., Kim E. J., Lukanidin E., Grigorian M. // Brit. J. Cancer. 2005. V. 92. № 11. P. 1955-1958.][Garrett S. C., Varney K. M., Weber D. J., Bresnick A. R. // J. Biol. Chem. 2006. V. 281. № 2. P. 677-680.][Schneider M., Hansen J. L., Sheikh S. P. // J. Mol. Med. 2008. V. 86. № 5. P. 507-522.][Grigorian M., Ambartsumian N., Lukanidin E. // Curr. Mol. Med. 2008. V. 8. № 6. P. 492-496.][Духанина Е. А., Лукьянова Т. И., Духанин А. С., Геор-гиева С. Г. // Бюл. эксперим. биологии и медицины. 2017. Т. 164. № 11. С. 614-616.][Chemaly E. R., Troncone L., Lebeche D. // Cell Calcium. 2018. V. 69. P. 46-61.][Духанина Е. А., Лукьянова Т. И., Романова Е. А., Духанин А. С., Сащенко Л. П. // Бюл. эксперим. биологии и медицины. 2008. Т. 145. № 1. С. 85-88.][Seth M., Sumbilla C., Mullen S. P., Lewis D., Klein M. G., Hussain A., Soboloff J., Gill D. L., Inesi G. // Proc. Natl. Acad. Sci. USA. 2004. V. 101. № 47. P. 16683-16688.][Lorenz S., Aust G., Krohn K. // Biochim. Biophys. Acta. 2013. V. 1833. № 12. P. 2703-2713.][Malashkevich V. N., Dulyaninova N. G., Ramagopal U. A., Liriano M. A., Varney K. M., Knight D., Brenowitz M., Weber D. J., Almo S. C., Bresnick A. R. // Proc. Natl. Acad. Sci. USA. 2010. V. 107. № 19. P. 8605-8610.][Andersen T. B., López C. Q., Manczak T., Martinez K., Simonsen H. T. // Molecules. 2015. V. 20. № 4. P. 6113-6127.]